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Crystallization and preliminary X-ray analysis of TBP-interacting protein from the hyperthermophilic archaeonThermococcus kodakaraensisstrain KOD1

Authors :
Shigenori Kanaya
Hiroyoshi Matsumura
Takahiko Yamamoto
Yasushi Kai
Tomoki Matsuda
Nami Sakamoto
Masaaki Morikawa
Tsuyoshi Inoue
Source :
Acta Crystallographica Section D Biological Crystallography. 59:372-374
Publication Year :
2003
Publisher :
International Union of Crystallography (IUCr), 2003.

Abstract

The 26 kDa TBP (TATA-binding protein) interacting protein from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 (Tk-TIP26) is a possible transcriptional regulatory protein in Thermococcales. Here, the crystallization of both the native and selenomethionine-substituted proteins and data collection are described. The native crystals belong to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = 73.83, c = 86.41 A, and diffract to 2.2 A using synchrotron radiation. MAD data was collected and a Bijvoet difference Patterson map showed strong peaks sufficient to determine the positions of the Se atoms.

Details

ISSN :
09074449
Volume :
59
Database :
OpenAIRE
Journal :
Acta Crystallographica Section D Biological Crystallography
Accession number :
edsair.doi.dedup.....3424f0648ef31427abfd777a1d240231
Full Text :
https://doi.org/10.1107/s090744490202142x